More Antibodies against Four and A Half LIM Domains 1 Interaction Partners

Human Four and A Half LIM Domains 1 (FHL1) interaction partners

Based on bioinformatic analysis, MMP1 and FHL1 are potentially functional proteins associated with differences of highly-metastatic prostate cancer PC-3M-1E8 cell line and poorly-metastatic PC-3M-2B4 cell line.

FHL1 can either suppress or promote tumor cell growth depending on the status of the sites for phosphorylation by Src.

FHL1 increase inhibitory CDC25 phosphorylation by forming a complex with CHK2 and CDC25, and sequester CDC25 in the cytoplasm by forming another complex with 14-3-3 and CDC25, resulting in increased radioresistance in cancer cells.

results provide evidence that FHL1A interacts with PLEKHG2 and regulates cell morphological change through the activity of PLEKHG2.

a novel FHL1 splice site variant results in the absence of FHL1A and the abundance of FHL1C, which may contribute to the complex and severe phenotype of Uruguay syndrome.

Knockdown of FHL1 with FHL1 small interfering RNA (siRNA) promoted tumor growth and Cyclin D and cyclin E were markedly elevated at both the protein and mRNA level.

results indicate that anti-FHL1 autoantibodies in peripheral blood have promising potential as a biomarker to identify a subset of severe IIM.

In healthy individuals, FHL1A is the predominant splice variant and is mainly found in skeletal and cardiac muscle. In two individuals with an Emery-Dreifuss plus phenotype with pulmonary artery hypoplasia and facial dysmorphology, there was demonstrated loss of isoform A and B, and an almost 200-fold overexpression of isoform C.

Our results suggest that miR-410 may function as an oncomiR and are consistent with its key function in regulating FHL1 in certain digestive system cancers.

These data suggested that up-regulated FHL1 in smooth muscle in HSCR might be associated with intestinal wall remodeling in HSCR and might be one of the risk factors for gastrointestinal motor dysfunction

This is the first study to show that FHL1 mutations identified in several clinically distinct myopathies lead to similar protein aggregation and impair myotube formation.

KyoT2 downregulates airway remodeling and resistance in asthmatic mice through a Hes1-dependent mechanism.

Results found that osteogenesis increases with the overexpression of Fhl1 and decreases with reduced Fhl1 expression and suggest that Fhl1 mediates interacting estrogen and Wnt signaling during osteogenesis.

Findings indicate that loss of function is responsible for the myopathy in the Fhl1 W122S knock-in mice.

The CSL-KyoT2 corepressor complex is a negative regulator of Notch signaling.

Data show that loss of FHL1 function leads to myopathy in vivo and suggest that loss of function of FHL1 may be one of the mechanisms underlying muscle dystrophy in patients with FHL1 mutations.

FHL1 is a novel regulator of myosin-binding protein C activity that may have a role in sarcomere assembly

These results suggest that KyoT2 is a substrate of SUMO modification catalyzed by PIAS1, and that SUMOylation may modulate the transcriptional repression effect of KyoT2 on the Notch/RBP-J signaling pathway.

significantly altered expression after short-term hypoxic exposure; identified as a novel protein regulated in various forms of pulmonary hypertension

KyoT3 is an isoform of murine FHL1, which associates with the transcription factor RBP-J and represses the RBP-J-mediated transactivation

four-and-a-half LIM domains 1 (FHL1) is part of a complex within the cardiomyocyte sarcomere that senses the biomechanical stress-induced responses important for cardiac hypertrophy.

FHL1 appears to modulate muscle mass and strength enhancement.

Data show that SLIMMER delayed Siva-1-dependent apoptosis in C2C12 myoblasts.

Four and A Half LIM Domains 1 (FHL1) Antigen Profile

Protein Summary

This gene encodes a member of the four-and-a-half-LIM-only protein family. Family members contain two highly conserved, tandemly arranged, zinc finger domains with four highly conserved cysteines binding a zinc atom in each zinc finger. Expression of these family members occurs in a cell- and tissue-specific mode and these proteins are involved in many cellular processes. Mutations in this gene have been found in patients with Emery-Dreifuss muscular dystrophy. Multiple alternately spliced transcript variants which encode different protein isoforms have been described.